ArticleThe Journal of biological chemistry2013
First crystal structure of a fungal high-redox potential dye-decolorizing peroxidase: substrate interaction sites and long-range electron transfer.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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36 citing papers in PubMed, 94 citations in OpenAlex.
- Exploring the biocatalytic potential of Amycolatopsis japonica DyP in degrading plasticizer and phenolic-derived xenobiotic compounds.Biodegradation · 2026Article
- Biochemical, Biophysical, and Structural Analysis of an Unusual DyP from the ExtremophileMolecules (Basel, Switzerland) · 2024Article
- New insights into controlling radical migration pathways in heme enzymes gained from the study of a dye-decolorising peroxidase.Chemical science · 2023Article
- Fungal dye-decolorizing peroxidase diversity: roles in either intra- or extracellular processes.Applied microbiology and biotechnology · 2022Article
- Direct Electrochemical Generation of Catalytically Competent Oxyferryl Species of Classes I and P Dye Decolorizing Peroxidases.International journal of molecular sciences · 2021Article
- Loops around the Heme Pocket Have a Critical Role in the Function and Stability ofInternational journal of molecular sciences · 2021Article
- Aspartate or arginine? Validated redox state X-ray structures elucidate mechanistic subtleties of FeJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021Review
- First Dye-Decolorizing Peroxidase from an Ascomycetous Fungus Secreted byBiomolecules · 2021Article
- Structural and Biochemical Characterization of a Dye-Decolorizing Peroxidase fromInternational journal of molecular sciences · 2021Article
- Mutational and structural analysis of an ancestral fungal dye-decolorizing peroxidase.The FEBS journal · 2021Article
- Revealing two important tryptophan residues with completely different roles in a dye-decolorizing peroxidase from Irpex lacteus F17.Biotechnology for biofuels · 2021Article
- Article
- MonokaryoticInternational journal of molecular sciences · 2021Article
- Understanding molecular enzymology of porphyrin-binding α + β barrel proteins - One fold, multiple functions.Biochimica et biophysica acta. Proteins and proteomics · 2021Review
- A DyP-Type Peroxidase ofMolecules (Basel, Switzerland) · 2020Article
- Resonance Raman view of the active site architecture in bacterial DyP-type peroxidases.RSC advances · 2020Review
- New insights on unspecific peroxygenases: superfamily reclassification and evolution.BMC evolutionary biology · 2019Article
- Linking Enzymatic Oxidative Degradation of Lignin to Organics Detoxification.International journal of molecular sciences · 2018Review
- A novel bacterial class V dye-decolourizing peroxidase from the extremophile Deinococcus radiodurans: cloning, expression optimization, purification, crystallization, initial characterization and X-ray diffraction analysis.Acta crystallographica. Section F, Structural biology communications · 2018Article
- Mechanism for the depolymerization of cellulose under alkaline conditions.Journal of molecular modeling · 2018Article
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Authors and funding
7 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Dye-decolorizing peroxidases (DyPs) belong to the large group of heme peroxidases. They utilize hydrogen peroxide to catalyze oxidations of various organic compounds. AauDyPI from Auricularia auricula-judae (fungi) was crystallized, and its crystal structure was determined at 2.1 Å resolution. The mostly helical structure also shows a β-sheet motif typical for DyPs and Cld (chlorite dismutase)-related structures and includes the complete polypeptide chain. At the distal side of the heme molecule, a flexible aspartate residue (Asp-168) plays a key role in catalysis. It guides incoming hydrogen peroxide toward the heme iron and mediates proton rearrangement in the process of Compound I formation. Afterward, its side chain changes its conformation, now pointing toward the protein backbone. We propose an extended functionality of Asp-168, which acts like a gatekeeper by altering the width of the heme cavity access channel. Chemical modifications of potentially redox-active amino acids show that a tyrosine is involved in substrate interaction. Using spin-trapping experiments, a transient radical on the surface-exposed Tyr-337 was identified as the oxidation site for bulky substrates. A possible long-range electron transfer pathway from the surface of the enzyme to the redox cofactor (heme) is discussed.
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